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Database: UniProt
Entry: A0A091K4D9_COLST
LinkDB: A0A091K4D9_COLST
Original site: A0A091K4D9_COLST 
ID   A0A091K4D9_COLST        Unreviewed;       545 AA.
AC   A0A091K4D9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=TNF receptor-associated factor {ECO:0000256|PIRNR:PIRNR015614};
DE            EC=2.3.2.27 {ECO:0000256|PIRNR:PIRNR015614};
GN   ORFNames=N325_10775 {ECO:0000313|EMBL:KFP30998.1};
OS   Colius striatus (Speckled mousebird).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Coliiformes; Coliidae; Colius.
OX   NCBI_TaxID=57412 {ECO:0000313|EMBL:KFP30998.1, ECO:0000313|Proteomes:UP000053615};
RN   [1] {ECO:0000313|EMBL:KFP30998.1, ECO:0000313|Proteomes:UP000053615}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N325 {ECO:0000313|EMBL:KFP30998.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900,
CC         ECO:0000256|PIRNR:PIRNR015614};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC       {ECO:0000256|ARBA:ARBA00004544}. Lipid droplet
CC       {ECO:0000256|ARBA:ARBA00004502}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the TNF receptor-associated factor family. A
CC       subfamily. {ECO:0000256|ARBA:ARBA00006608}.
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DR   EMBL; KK541470; KFP30998.1; -; Genomic_DNA.
DR   RefSeq; XP_010198443.1; XM_010200141.1.
DR   AlphaFoldDB; A0A091K4D9; -.
DR   GeneID; 104556332; -.
DR   KEGG; csti:104556332; -.
DR   CTD; 7189; -.
DR   OrthoDB; 2913784at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000053615; Unassembled WGS sequence.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005164; F:tumor necrosis factor receptor binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:UniProt.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR   GO; GO:0043122; P:regulation of canonical NF-kappaB signal transduction; IEA:InterPro.
DR   CDD; cd03776; MATH_TRAF6; 1.
DR   CDD; cd16643; mRING-HC-C3HC3D_TRAF6; 1.
DR   Gene3D; 1.20.5.340; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
DR   InterPro; IPR002083; MATH/TRAF_dom.
DR   InterPro; IPR012227; TNF_rcpt-assoc_TRAF_met.
DR   InterPro; IPR008974; TRAF-like.
DR   InterPro; IPR037309; TRAF6_MATH.
DR   InterPro; IPR027139; TRAF6_RING-HC.
DR   InterPro; IPR041310; TRAF6_Z2.
DR   InterPro; IPR049342; TRAF_MEP1_MATH_dom.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   InterPro; IPR001293; Znf_TRAF.
DR   PANTHER; PTHR10131; TNF RECEPTOR ASSOCIATED FACTOR; 1.
DR   PANTHER; PTHR10131:SF94; TNF RECEPTOR-ASSOCIATED FACTOR 6; 1.
DR   Pfam; PF21355; TRAF-mep_MATH; 1.
DR   Pfam; PF18048; TRAF6_Z2; 1.
DR   Pfam; PF13923; zf-C3HC4_2; 1.
DR   Pfam; PF02176; zf-TRAF; 1.
DR   PIRSF; PIRSF015614; TRAF; 1.
DR   SMART; SM00061; MATH; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF49599; TRAF domain-like; 3.
DR   PROSITE; PS50144; MATH; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   PROSITE; PS50145; ZF_TRAF; 2.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR015614};
KW   Lipid droplet {ECO:0000256|ARBA:ARBA00022677};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR015614}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Receptor {ECO:0000313|EMBL:KFP30998.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053615};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR015614};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00207}.
FT   DOMAIN          70..109
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          151..199
FT                   /note="TRAF-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50145"
FT   DOMAIN          204..258
FT                   /note="TRAF-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50145"
FT   DOMAIN          373..522
FT                   /note="MATH"
FT                   /evidence="ECO:0000259|PROSITE:PS50144"
FT   ZN_FING         151..199
FT                   /note="TRAF-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00207"
FT   ZN_FING         204..258
FT                   /note="TRAF-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00207"
FT   COILED          315..370
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   545 AA;  62105 MW;  1133FB37AF09E307 CRC64;
     MSLLHSDSSC GARDMESGCC AAMASACSVG AKEDSVSVSS STANPPSSFT EETQGYDVEF
     DPPLESKYEC PICLMALREA VQTPCGHRFC KGCIVKSIRD AGHKCPVDNE ILLENQLFPD
     NFAKREILSL TVKCPNKGCS MKMELRHLED HQLQCDFSTV ECPQCQGAFQ KNHLKEHMTQ
     ECLRRQVCCP NCATSMAYED KELHDQTCPL ANVFCEYCNT MLIREQMPNH YDNDCPTAPV
     PCFYSAFGCP EKMQRNELAR HMQEFTQVHM RMMAQSFQNI SVTAANPVPF LNGLPFEPAF
     LSHVSHAPYN CNPDVENFKE TIHQLEGRLV RQDHQIRELI AKMETQNTHV AELKRTIRSL
     EGKITEMEAQ QCNGIYIWKI ENFSELQKAQ EEERPVVMHS PGFYTGKPGY KLCLRLHIQL
     PNAQRCANFI SLFVHTMQGE YDSHLPWPFQ GTIRLSILDQ SEGPDRQNHE EVMEAKPELL
     AFQRPTIHRN PKGFGYVTFM HLQTLKQRTF VKDDTLLVRC EVLTRLDLSS LRREGFQPRS
     TDGTL
//
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